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2013 | 60 | 4 | 553-564
Article title

A computational approach to structural properties of glycoside hydrolase family 4 from bacteria

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EN
Abstracts
EN
Structural bioinformatics approaches applied to the alpha- and beta-glycosidases from the GH4 enzyme family reveal that, despite low sequence identity, these enzymes possess quite similar global structural characteristics reflecting a common reaction mechanism. Locally, there are a few distinctive structural characteristics of GH4 alpha- and beta-glycosidases, namely, surface cavities with different geometric characteristics and two regions with highly dissimilar structural organizations and distinct physicochemical properties in the alpha- and beta-glucosidases from Thermotoga maritima. We suggest that these structurally dissimilar regions may be involved in specific protein-protein interactions and this hypothesis is sustained by the predicted distinct functional partners of the investigated proteins. Also, we predict that alpha- and beta-glycosidases from the GH4 enzyme family interact with difenoconazole, a fungicide, but there are different features of these interactions especially concerning the identified structurally distinct regions of the investigated proteins.
Publisher

Year
Volume
60
Issue
4
Pages
553-564
Physical description
Dates
published
2013
received
2013-01-27
revised
2013-10-02
accepted
2013-12-06
(unknown)
2013-12-16
Contributors
author
  • West University of Timisoara, Teacher Training Department, Timisoara, Romania
  • West University of Timisoara, Department of Biology and Chemistry, Timisoara, Romania
  • West University of Timisoara, Department of Biology and Chemistry, Timisoara, Romania
author
  • West University of Timisoara, Department of Biology and Chemistry, Timisoara, Romania
  • West University of Timisoara, Department of Biology and Chemistry, Timisoara, Romania
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv60p553kz
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